ALPHA-GALACTOSIDASE FROM ALFALFA SEEDS (MEDICAGO-SATIVA L)

An α-galactosidase from alfalfa seeds was purified 140-fold by ammonium sulfate fractionation, and column chromatography on Sephadex G-100, DEAE- and CM-Sephadex. Polyacrylamide-gel electrophoresis of the purified enzyme showed a single protein band. The molecular weight was estimated to be approximately 57, 000 by gel-filtration. The purified enzyme hydrolyzed p-nitrophenyl α-D-galactoside more rapidly than raffinose. The maximal enzyme activities were obtained at pH 4.0 and 5.5 for p-nitrophenyl α-D-galactoside and at 4.5 for raffinose. The enzyme was shown to be inhibited by Hg2+ and Ag+ ions, and D-galactose. © 1979 Taylor and Francis Group, LLC.